Chemists and microbiologists are making progress studying supramolecular interactions - noncovalent forces that direct the assembly of molecules - that occur in bacterial exoskeletons. Because peptidoglycan is the key structural component of the bacterial exoskeleton, how its constituent molecules are assembled into a three-dimensional molecular edifice is one of the most challenging problems in microbiology. The peptidoglycan structure is dynamic, with 40-45% of its structure released and recycled during each growth cycle; its glycan strands in E. coli consist of two ensembles, one shorter and one longer. Based on several analyses, including of single glycan strands, the Escherichia coli peptidoglycan glycan backbones appear to run perpendicular to the cell surface, forming a honeycombed structure that is full of pores studded with proteins.
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